GSBS Student Publications

Title

Binding of radioiodinated influenza virus peptides to class I MHC molecules and to other cellular proteins as analyzed by gel filtration and photoaffinity labeling

UMMS Affiliation

Graduate School of Biomedical Sciences; Department of Pharmacology

Date

4-1-1991

Document Type

Article

Medical Subject Headings

Affinity Labels; Amino Acid Sequence; Antigens, Viral; Binding, Competitive; Cell Line; Chromatography, Gel; HLA-B Antigens; Histocompatibility Antigens Class I; Humans; Membrane Proteins; Microsomes; Molecular Sequence Data; Nucleoproteins; Orthomyxoviridae; Peptides; Viral Matrix Proteins

Disciplines

Life Sciences | Medicine and Health Sciences

Abstract

In order to determine how T cell-presented peptides associate with the antigen binding sites (desetopes) of class I major histocompatibility complex (MHC) molecules and how they might be scavenged from an endogenous processing pathway for transfer to those molecules, we characterized the binding of two synthetic peptides restricted by HLA-B37 or HLA-A2 to class I MHC molecules and to cellular proteins of histotyped cell lines, by gel filtration and photo-affinity labeling techniques. In gel filtration binding studies, each peptide associated with immunopurified class I MHC molecules from cells with its restricting, histotype, but little was bound to class I MHC molecules from cells without the restricting histotype and none was bound to bovine serum albumin. After crosslinkage of a radioiodinated photoreactive derivative of influenza virus nucleoprotein peptide NP(336-355Y) and immunoprecipitations with antibodies to class I MHC molecules, that peptide was found to bind to immunopurified class I MHC molecules from HLA-B37+ but not HLA-B37- cells. Binding of the [125I]NP peptide increased from 6 to 12 hr of incubation and was competed by unlabeled, NP peptide but not by HLA-A2-restricted, influenza virus matrix MA(57-73). The principal microsomal membrane proteins binding [125I]NP were about 65, 45 and 33 kD.

Rights and Permissions

Citation: Mol Immunol. 1991 Apr-May;28(4-5):341-8.

Related Resources

Link to Article in PubMed

Journal Title

Molecular immunology

PubMed ID

2062316